Please use this identifier to cite or link to this item:
http://hdl.handle.net/1893/11279
Appears in Collections: | Aquaculture Journal Articles |
Peer Review Status: | Refereed |
Title: | Molecular characterization, expression and localization of a peroxiredoxin from the sheep scab mite, Psoroptes ovis |
Author(s): | McNair, Carol Nisbet, Alasdair Billingsley, Peter Knox, David |
Contact Email: | c.m.mcnair@stir.ac.uk |
Keywords: | Psoroples ovis antioxidant immunity reactive oxygen species |
Issue Date: | Apr-2009 |
Date Deposited: | 4-Mar-2013 |
Citation: | McNair C, Nisbet A, Billingsley P & Knox D (2009) Molecular characterization, expression and localization of a peroxiredoxin from the sheep scab mite, Psoroptes ovis. Parasitology, 136 (4), pp. 453-460. https://doi.org/10.1017/S0031182009005538 |
Abstract: | The sheep scab mite, Psoroptes ovis, induces an intensely pruritic exudative dermatitis which is responsible for restlessness, loss of appetite and weight loss. Within the first 24 h of infection, there is a rapid inflammatory influx of eosinophils and apoptosis of the keratinocytes at the site of infection. The former cell type is capable of a sustained respiratory burst, toxic products of which may directly damage the mite and also contribute to lesion formation. Analysis of a P. ovis expressed sequence tag (EST) database identified a number of antioxidant enzyme-encoding sequences, including peroxiredoxin (thioredoxin peroxidase EC 1.11.1.15), all of which may help the mite endure the potentially toxic skin environment. A full length sequence encoding Po-TPx, a protein of 206 amino acids which showed high homology to a peroxiredoxin from the salivary gland of the tick Ixodes scapularis, was amplified from P. ovis cDNA. Recombinant Po-TPx was expressed in bacteria and antiserum to this protein was used to localize native Po-TPx in mite sections. Peroxiredoxin was localized, amongst other sites, to a subpharyngeal region in mite sections. The recombinant protein was recognized by sera from sheep infested with the mite suggesting that it may be secreted or excreted by the mite and interact with the host immune response. |
DOI Link: | 10.1017/S0031182009005538 |
Rights: | Publisher policy allows this work to be made available in this repository. Published in Parasitology / Volume 136 / Issue 04 / April 2009, pp 453-460 Copyright © 2009 Cambridge University Press. The original publication is available at http://dx.doi.org/10.1017/S0031182009005538 |
Files in This Item:
File | Description | Size | Format | |
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TPX.pdf | Fulltext - Published Version | 188.04 kB | Adobe PDF | View/Open |
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